Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction

quantum chemical study of the imine formation reaction, which precedes P-C bond cleavage. The barrier of this reaction can be significantly lowered if the reaction is assisted by a water molecule and the substrate is protonated

Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction

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SYSTEMATIC NAME

IUBMB Comments

2-oxoethylphosphonate phosphonohydrolase

This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the haloacetate dehalogenase family.

strain IFO 12010. 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied

strain IFO 12010. 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied

strain NG2, can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium

strain NG2, can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium

the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes

the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon

the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR

the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR

the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon

the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes

the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR

the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile

the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile

the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile

the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile

the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile

activates, required for catalysis, serves as a cofactor, binds via ligation to the loop 1 Asp12 carboxylate and Thr 14 backbone carbonyl and to the loop 4 Asp186carboxylate, the loop 4 Asp190 forms a hydrogen bond to the Mg(II) water ligand, Asp186 is essential while Asp190 simply enhances cofactor binding